Structural Basis for the Receptor Binding Specificity of Norwalk Virus - Wikidata - awgldk - TriplyDB

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

http://www.wikidata.org/entity/Q27650214

about

Conservation of carbohydrate binding interfaces: evidence of human HBGA selection in norovirus evolution Structural basis of glycan interaction in gastroenteric viral pathogens Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure High-Resolution X-Ray Structure and Functional Analysis of the Murine Norovirus 1 Capsid Protein Protruding Domain Crystal Structures of GII.10 and GII.12 Norovirus Protruding Domains in Complex with Histo-Blood Group Antigens Reveal Details for a Potential Site of Vulnerability Structural Analysis of Histo-Blood Group Antigen Binding Specificity in a Norovirus GII.4 Epidemic Variant: Implications for Epochal Evolution Crystallography of a Lewis-Binding Norovirus, Elucidation of Strain-Specificity to the Polymorphic Human Histo-Blood Group Antigens Structural Basis for Norovirus Inhibition and Fucose Mimicry by Citrate Structural Basis for Broad Detection of Genogroup II Noroviruses by a Monoclonal Antibody That Binds to a Site Occluded in the Viral Particle Pathogenesis of noroviruses, emerging RNA viruses Inhibition of histo-blood group antigen binding as a novel strategy to block norovirus infections Rabbit haemorrhagic disease (RHD) and rabbit haemorrhagic disease virus (RHDV): a review Antiviral targets of human noroviruses Expression of the murine norovirus (MNV) ORF1 polyprotein is sufficient to induce apoptosis in a virus-free cell model.Vaccine against norovirus.Genetic diversity and histo-blood group antigen interactions of rhesus enteric caliciviruses.Heterotypic humoral and cellular immune responses following Norwalk virus infection.Norovirus gastroenteritis, carbohydrate receptors, and animal models.Targeting norovirus infection-multivalent entry inhibitor design based on NMR experiments.Divergent evolution of norovirus GII/4 by genome recombination from May 2006 to February 2009 in Japan.Branched-linear and agglomerate protein polymers as vaccine platforms.Genetic and phenotypic characterization of GII-4 noroviruses that circulated during 1987 to 2008.Susceptibility to winter vomiting disease: a sweet matter.Genogroup IV and VI canine noroviruses interact with histo-blood group antigens.Identification of human single-chain antibodies with broad reactivity for noroviruses.Affinities of recombinant norovirus P dimers for human blood group antigens Two gastroenteritis outbreaks caused by GII Noroviruses: host susceptibility and HBGA phenotypes Norovirus P particle efficiently elicits innate, humoral and cellular immunity Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles Isolation of cross-reactive human monoclonal antibodies that prevent binding of human noroviruses to histo-blood group antigens.Crystal structures of GI.8 Boxer virus P dimers in complex with HBGAs, a novel evolutionary path selected by the Lewis epitope.Norovirus-host interaction: multi-selections by human histo-blood group antigens.Affinities of human histo-blood group antigens for norovirus capsid protein complexes.Antigenic Relatedness of Norovirus GII.4 Variants Determined by Human Challenge Sera A Unique Human Norovirus Lineage with a Distinct HBGA Binding Interface.Tulane virus recognizes sialic acids as cellular receptors.Elucidation of strain-specific interaction of a GII-4 norovirus with HBGA receptors by site-directed mutagenesis study.Noroviral P particle: structure, function and applications in virus-host interaction.Norovirus P particle: a subviral nanoparticle for vaccine development against norovirus, rotavirus and influenza virus.Mechanism of Cell Culture Adaptation of an Enteric Calicivirus, the Porcine Sapovirus Cowden Strain.

P2860

Q21143806-82F8B88E-2C35-4654-9E27-B93748FB0E52 Q27030776-DF3818BC-0B67-4092-A230-FF2B3A863732 Q27646563-92607067-8D71-4EDE-862A-22AF752CF334 Q27660321-54E98E40-2D7C-47C9-91F9-B42E788F85C6 Q27667594-3DE7B8BB-4AF6-45EA-B819-FCE97BC37D5D Q27670610-035CE5DE-ABC1-483E-8818-AC48FC301862 Q27671411-278438A5-4EC8-43CD-B11F-30143F032F2B Q27675252-AE312EB1-4B1F-4B14-B5BE-A644DA0B47F4 Q27676892-3DD68A0A-F526-4FF5-A626-7F8B338F00EE Q28392368-35C2EDB6-CB0B-409C-831A-7F061CCBD4A0 Q28534736-4799BC67-4DCB-4DCD-86A5-65BBFBA0CDEA Q28730482-F866CDEF-5BC9-42C6-A38F-38A3CFB2DFC2 Q30249527-994670C7-68C9-4FED-A286-69CB5DC60F01 Q31153401-31216303-E9A3-4E1A-8A57-A0062CD80B52 Q33578075-9A9D438D-BD65-4B41-B732-663A560C86B4 Q33606705-207B6D1E-6B0B-451A-A00F-A91EA50FCD28 Q33614589-1BF83916-D112-46DF-931F-E934FD053642 Q33701801-56A99EBC-817F-4C2E-8B49-C91567F37F46 Q33897924-E88EF2DA-AE41-4F6D-BD57-6826B085C6C7 Q34046026-4D22A561-D3A0-47B3-B412-51AAC3BA2A18 Q34064413-91E21285-851C-4682-A764-005CDD7BA5B7 Q34120230-0F7CA35D-6379-4812-B4AF-0FE3353F64A6 Q34227237-637264CA-557C-436C-84EF-8070465D2268 Q34262016-5C6DC3AF-2E0D-4D75-A5F9-0802ACEB8049 Q34313167-D4413046-34AD-476F-BB91-8E1EAF1A1853 Q34464196-1BB7FB3A-4C31-4A3B-B4AF-9660BAE86C35 Q34615059-AE0F7BFE-7349-4FC3-92BB-7F28430BFF37 Q34702360-CF44408D-B737-4C39-BA2C-1043371A54C4 Q34724844-2BC41164-23F7-4C2C-8D08-9030A40126AB Q34985473-2F4AF415-3054-4949-A6D5-5A2DDA52C28D Q35034538-B5DC9687-1081-445D-BC5E-324E5128C9B8 Q35146233-F2F8E0CE-3655-4D27-BD4F-2D99418BD23E Q35152899-B7644E42-3BD3-4D94-979A-37F4B31F82A4 Q35615462-609B5AF7-04ED-41E0-852F-5B2499E8B6E4 Q35683789-714A9B3E-523B-4517-B82B-F02EF38854A0 Q35819128-2A5ADAD6-B6EE-48F8-85B2-4BFEBEF460F9 Q36415015-20890C42-00FB-4048-B181-55422140F994 Q36429481-A3367761-F180-4F2F-9A01-DEF62715DBB1 Q36445296-37EF2EDF-53BF-4287-BB92-3CD10C325AD4 Q36481493-255EA3A3-47FC-404D-8A02-599C243AF038

P2860

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

http://www.wikidata.org/entity/Q27650214

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@ast

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@en

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@nl

type

label

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@ast

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@en

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@nl

prefLabel

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@ast

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@en

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@nl

P1433

Q27650214-777125E4-0918-4132-ABE5-54C354880EC7

P1476

Q27650214-DC88B02F-C53E-48D4-A831-8F08DA3357A4

P2093

Q27650214-1404230F-9724-4001-A7BE-DC58D80AC3EA

Q27650214-2246D838-B2FA-4903-B09B-5A534264247B

Q27650214-35CC42CA-00DE-4D88-BC1D-27E31A81E33B

Q27650214-C93CA8D5-5E11-4D4A-A01F-4126A5A6928D

Q27650214-D03F0B96-1B22-4345-8EED-3C3782EF9685

Q27650214-D5F8C2DE-9C63-4638-AA07-2D0D5D6B0E71

P2860

Q27650214-07A6EFDE-00BF-489C-A261-BCAECF4ED30A

Q27650214-187F5205-E194-4875-B86D-112DB2D134A6

Q27650214-19B3F342-C0C3-47B5-B105-485D73C606D1

Q27650214-2108C335-5187-4414-81EC-682C8BD5E199

Q27650214-24BF83A9-9717-49A9-B708-18259126C05A

Q27650214-315807E4-A2F5-4DF4-97B5-34C35E769E17

Q27650214-3D36850C-04B6-49A0-999B-15E7E873F9A1

Q27650214-50D13753-1672-46BC-AD63-E127C622BE19

Q27650214-5FE6EF88-CC5F-435B-A6AF-1E4E1EF64D8A

Q27650214-9F63ABEF-C123-4BDC-A9BD-D0423914BABE

P304

Q27650214-A5D8FF3F-68B6-444A-866E-8732F08AF12F

P31

Q27650214-676719DC-9AE2-4BD3-9505-18D68D90DD1B

P356

Q27650214-80B12789-BE6A-4841-A712-F25726B6488B

P433

Q27650214-C6BB3D64-8D36-4699-BE95-E6C0DA12749F

P478

Q27650214-B60C63E7-7877-49FC-8705-8F0A44D80530

P577

Q27650214-EEEEA092-E9B6-4C88-82CE-C2E43AFC20BB

P698

Q27650214-D04CBF86-B728-4BAA-967E-A8E4953E7FC5

P921

Q27650214-B9B49A02-D66C-44ED-8214-091B37C1FA90

P932

Q27650214-7B8E358A-04B5-4B3F-9873-8A1D70189096

P356

P1433

Journal of Virology

P1476

Structural Basis for the Receptor Binding Specificity of Norwalk Virus

@en

P2093

Aygun Mamedova

http://www.w3.org/2001/XMLSchema#string

Ming Tan

http://www.w3.org/2001/XMLSchema#string

Ming Xia

http://www.w3.org/2001/XMLSchema#string

Rashmi S Hegde

http://www.w3.org/2001/XMLSchema#string

Weiming Bu

http://www.w3.org/2001/XMLSchema#string

Xi Jiang

http://www.w3.org/2001/XMLSchema#string

P2860

The P domain of norovirus capsid protein forms dimer and binds to histo-blood group antigen receptors

Structural basis for the recognition of blood group trisaccharides by norovirus

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

X-ray crystallographic structure of the Norwalk virus capsid

ESPript: analysis of multiple sequence alignments in PostScript

Knowledge-based protein secondary structure assignment

Norovirus and its histo-blood group antigen receptors: an answer to a historical puzzle.

The p domain of norovirus capsid protein forms a subviral particle that binds to histo-blood group antigen receptors.

Structural requirements for the assembly of Norwalk virus-like particles

P304

5340-7

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1128/JVI.00135-08

http://www.w3.org/2001/XMLSchema#string

P433

11

http://www.w3.org/2001/XMLSchema#string

P478

82

http://www.w3.org/2001/XMLSchema#string

P577

2008-06-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

18385236

http://www.w3.org/2001/XMLSchema#string

P921

P932

2395213

http://www.w3.org/2001/XMLSchema#string